Purification of Phosphoinositol Kinase from Suspension-cultured Cells of Rice (Oryza sativa L.)
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概要
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Phosphoinositol kinase was purified from suspension-cultured rice (Oryza sativa L. ) cells. The apparent molecular mass of the rice enzyme was estimated to be 58kDa by SDS-PAGE and 234kDa by Toyopearl HW-55S gel filtration, indicating that it is a tetrameric enzyme. The enzyme absolutely required Mg2+ for the activity, but Mn2 + and Ca2 + did not affect it. In addition, this kinase phosphorylated inositol monophosphate to phytate. Judging from these data, rice phosphoinositol kinase was concluded to be a different enzyme distinguished from the other plant phosphoinositol kinases.
- 社団法人日本農芸化学会の論文
- 1995-10-23
著者
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MITSUI Toshiaki
Department of Applied Biological Chemistry, Faculty of Agriculture and Graduate School of Science an
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Mitsui Toshiaki
Department Of Applied Biological Chemistry Faculty Of Agriculture Niigata University
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Mitsui Toshiaki
Department Of Agricultural Chemistry Faculty Of Agriculture Niigata University
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HAYAKAWA Toshiro
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University
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Yotsushima Kenji
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University
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Hayakawa T
Department Of Applied Biological Chemistry Faculty Of Agriculture Niigata University
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Hayakawa Toshiro
Department Of Agricultural Chemistry Faculty Of Agriculture Niigata University
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Yotsushima K
Toyama Prefectural Agricultural Research Center
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